Phospho-Ubiquitin (Ser65) Rabbit Monoclonal Antibody for WB, IF/ICC, ELISA - P62979 / P62987 / P0CG47 / P0CG48

Core Product Specifications and Parameters

Biological Background: Ubiquitin Function and Localization

• Ubiquitin is a highly conserved 76‑amino acid protein, often expressed as a fusion protein with ribosomal protein eS31 (gene RPS27A) and cleaved to generate free ubiquitin and the ribosomal component.
• Ubiquitin can be conjugated to target proteins via isopeptide bonds, forming monomers or polyubiquitin chains linked through different lysine residues; Lys‑48‑linked chains target proteins for proteasomal degradation, while Lys‑63‑linked chains mediate endocytosis, DNA repair, and NF‑κB signaling.
• As part of the 40S ribosomal subunit, the ubiquitin‑ribosomal fusion protein participates in ribosome biogenesis and pre‑rRNA processing within the nucleolus. Related references: PMID:9582194, PMID:23636399, PMID:34516797
• Ubiquitin undergoes various post‑translational modifications, including phosphorylation, acetylation, and ADP‑ribosylation, which modulate its cellular functions.
• The fusion protein also acts as a zinc‑binding ribosomal protein, containing a C4‑type zinc finger motif.
• Subcellular localization includes the cytoplasm, nucleus, and nucleolus, consistent with roles in both cytosolic protein degradation and nuclear ribosome assembly.

Experimental Guidance and Technical Tips

• Due to the labile nature of phosphorylation, include phosphatase inhibitors during sample preparation to preserve the phospho‑Ser65 epitope.
• Verify antibody specificity by phosphatase treatment of lysates or by competing with a non‑phosphorylated peptide.
• Multiple bands may be detected because ubiquitin is conjugated to numerous target proteins; predicted molecular weights include free ubiquitin (~8.5 kDa) and higher‑molecular‑weight conjugates (observed bands at ~15, 18, 26, and 77 kDa).
• For immunofluorescence, optimize fixation and permeabilization conditions to retain the phosphorylation signal.

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